Information on EC 2.4.2.54 - beta-ribofuranosylphenol 5'-phosphate synthase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
2.4.2.54
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RECOMMENDED NAME
GeneOntology No.
beta-ribofuranosylphenol 5'-phosphate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-phospho-alpha-D-ribose 1-diphosphate + 4-hydroxybenzoate = 4-(beta-D-ribofuranosyl)phenol 5'-phosphate + CO2 + diphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tetrahydromethanopterin biosynthesis
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tetrahydrofolate metabolism
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SYSTEMATIC NAME
IUBMB Comments
5-phospho-alpha-D-ribose 1-diphosphate:4-hydroxybenzoate 5-phospho-beta-D-ribofuranosyltransferase (decarboxylating)
The enzyme is involved in biosynthesis of tetrahydromethanopterin in archaea. It was initially thought to use 4-aminobenzoate as a substrate, but was later shown to utilize 4-hydroxybenzoate [4]. The activity is dependent on Mg2+ or Mn2+ [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-aminobenzoate + 5-phospho-alpha-D-ribose 1-diphosphate
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + CO2 + diphosphate
show the reaction diagram
5-phospho-alpha-D-ribose 1-diphosphate + 4-aminobenzoate
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + CO2 + diphosphate
show the reaction diagram
5-phospho-alpha-D-ribose 1-diphosphate + 4-aminobenzoate
4-(beta-D-ribofuranosyl)aniline 5'-phosphate + CO2 + diphosphate
show the reaction diagram
5-phospho-alpha-D-ribose 1-diphosphate + 4-hydroxybenzoate
4-(beta-D-ribofuranosyl)hydroxybenzene 5'-phosphate + CO2 + diphosphate
show the reaction diagram
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sequential pattern of substrate binding
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-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-aminobenzoate + 5-phospho-alpha-D-ribose 1-diphosphate
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + CO2 + diphosphate
show the reaction diagram
O28190
the enzyme is involved in biosynthesis of tetrahydromethanopterin, a folate analog involved in the C1 metabolism of methanogenic archaea, sulfate-reducing archaea, and methylotrophic bacteria
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?
5-phospho-alpha-D-ribose 1-diphosphate + 4-aminobenzoate
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate + CO2 + diphosphate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
the enzyme lacks any chromogenic cofactor, and the presence of pyridoxal phosphate and the mechanistically related pyruvoyl cofactors is excluded
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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reaction is dependent on Mg2+ or Mn2+, optimal concentration: 10 mM
Mn2+
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reaction is dependent on Mg2+ or Mn2+
additional information
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requires no dissociable trace metal ions such as iron or cobalt ion for activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate
uncompetitive inhibition under varied 5-phospho-alpha-D-ribose 1-diphosphate and saturated 4-aminobenzoate or under varied 4-aminobenzoate and saturated 5-phospho-alpha-D-ribose 1-diphosphate
4-(methylamino)benzoic acid
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5 mM, complete loss of activity
4-aminothiobenzoate
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5 mM, 24% loss of activity
4-Bromobenzoate
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5 mM, 60% loss of activity
4-hydroxybenzoate
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5 mM, 88% loss of activity
4-Methoxybenzoate
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5 mM, 55% loss of activity
4-methylaminobenzoate
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5 mM, 26% inhibition
Benzoate
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5 mM, 31% loss of activity
CO2
uncompetitive inhibition under varied 5-phospho-alpha-D-ribose 1-diphosphate and saturated 4-aminobenzoate. Mixed type of inhibition under varied 4-aminobenzoate and saturated 5-phospho-alpha-D-ribose 1-diphosphate
diphosphate
phosphate
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10 mM, 37% inhibition
pyridoxal 5'-phosphate
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2.5 mM, 21% inhibition
ribose 5-phosphate
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10 mM, 20% inhibition
Sodium cyanoborohydride
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160 mM, complete inhibition, decreased production of 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate and the accumulation of a reduced form of the proposed cyclohexadienimine reaction intermediates
additional information
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no inhibition by carbonyl reagents, 4-aminobenzoic acid methyl ester, aniline, 4-aminobenzamide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.058 - 0.15
4-Aminobenzoate
1.5 - 3.6
5-phospho-alpha-D-ribose 1-diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
5-phospho-alpha-D-ribose 1-diphosphate
Methanocaldococcus jannaschii
Q58822
pH 4.8, 70C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 0.3
4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate
0.59
4-Bromobenzoate
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pH 4.8, 50C, Ki(slope)
0.07
4-hydroxybenzoate
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pH 4.8, 50C, Ki(slope)
0.99
CO2
pH 4.8, 70C, uncompetitive inhibition under varied 5-phospho-alpha-D-ribose 1-diphosphate and saturated 4-aminobenzoate
0.32
diphosphate
pH 4.8, 70C, competitive inhibition under saturated 5-phospho-alpha-D-ribose 1-diphosphate and varied 4-aminobenzoate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03
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pH 4.8, 50C
0.075
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50C, pH 5.0
0.29
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50C, pH 5.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
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gel filtration
64500
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gel filtration
65000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 36200, SDS-PAGE
monomer
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1 * 64000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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the activity of the enzyme pretreated for 30 min at pH 4.0 is 48% of the activity for enzyme treated at either pH 4.8 or 5.9
718828
4.8
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the activity of the enzyme pretreated for 30 min at pH 4.0 is 48% of the activity for enzyme treated at either pH 4.8 or 5.9
718828
5.9
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the activity of the enzyme pretreated for 30 min at pH 4.0 is 48% of the activity for enzyme treated at either pH 4.8 or 5.9
718828
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2 mM dithiothreitol and 10% (v/v) glycerol stabilize the enzyme activity during long-term storage and subsequent purification steps
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
relatively stable in air
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718828
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
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